Results 1 to 10 of about 10,680,823 (279)

The Substrate Specificity of Sirtuins

open access: yesAnnual Review of Biochemistry, 2016
Sirtuins are NAD+-dependent enzymes universally present in all organisms, where they play central roles in regulating numerous biological processes. Although early studies showed that sirtuins deacetylated lysines in a reaction that consumes NAD+, more recent studies have revealed that these enzymes can remove a variety of acyl-lysine modifications ...
Bheda, P.   +3 more
openaire   +4 more sources

The intrinsic substrate specificity of the human tyrosine kinome. [PDF]

open access: yesNature
Phosphorylation of proteins on tyrosine (Tyr) residues evolved in metazoan organisms as a mechanism of coordinating tissue growth1. Multicellular eukaryotes typically have more than 50 distinct protein Tyr kinases that catalyse the phosphorylation of ...
Yaron-Barir TM   +35 more
europepmc   +2 more sources

Structural basis for substrate specificity of mammalian neuraminidases.

open access: yesPLoS ONE, 2014
The removal of sialic acid (Sia) residues from glycoconjugates in vertebrates is mediated by a family of neuraminidases (sialidases) consisting of Neu1, Neu2, Neu3 and Neu4 enzymes.
Victoria Smutova   +7 more
doaj   +2 more sources

Probabilistic approach to predicting substrate specificity of methyltransferases.

open access: yesPLoS Computational Biology, 2014
We present a general probabilistic framework for predicting the substrate specificity of enzymes. We designed this approach to be easily applicable to different organisms and enzymes.
Teresa Szczepińska   +7 more
doaj   +2 more sources

Phage-assisted continuous evolution of proteases with altered substrate specificity

open access: yesNature Communications, 2017
Proteases are promising therapeutics to treat diseases such as hemophilia which are due to endogenous protease deficiency. Here the authors use phage-assisted continuous evolution to evolve a variant TEV protease with altered target peptide sequence ...
Michael S. Packer   +2 more
doaj   +2 more sources

Structural basis of SIRT7 nucleosome engagement and substrate specificity [PDF]

open access: yesNature Communications
Chromatin-modifying enzymes target distinct residues within histones to finetune gene expression profiles. SIRT7 is an NAD+-dependent deacylase often deregulated in cancer, which deacetylates either H3 lysine 36 (H3K36) or H3K18 with high specificity ...
Carlos Moreno-Yruela   +6 more
doaj   +3 more sources

Substrate Specificity in Thiol Dioxygenases

open access: yesBiochemistry, 2019
Thiol dioxygenases make up a class of ferrous iron-dependent enzymes that oxidize thiols to their corresponding sulfinates. X-ray diffraction structures of cysteine-bound cysteine dioxygenase show how cysteine is coordinated via its thiolate and amine to the iron and oriented correctly for O atom transfer.
Sekotilani Aloi   +4 more
openaire   +3 more sources

Discovery and substrate specificity engineering of nucleotide halogenases [PDF]

open access: yesNature Communications
C2′-halogenation has been recognized as an essential modification to enhance the drug-like properties of nucleotide analogs. The direct C2ʹ-halogenation of the nucleotide 2′-deoxyadenosine-5′-monophosphate (dAMP) has recently been achieved using the Fe ...
Jie Ni   +4 more
doaj   +2 more sources

Structural Analysis and Substrate Specificity of D-Carbamoylase from Pseudomonas [PDF]

open access: yesBioTech
The synthesis of enantiomeric forms of D-amino acids can be achieved by a two-step “hydantoinase process” based on the sequential catalysis of substrates by specific enzymes, D-carbamoylase and D-hydantoinase. Here, we describe the structural features of
Marina Paronyan   +9 more
doaj   +2 more sources

Substrate Specificity of SARS-CoV-2 Nsp10-Nsp16 Methyltransferase

open access: yesViruses, 2021
The ongoing COVID-19 pandemic exemplifies the general need to better understand viral infections. The positive single-strand RNA genome of its causative agent, the SARS coronavirus 2 (SARS-CoV-2), encodes all viral enzymes.
Roberto Benoni   +5 more
doaj   +1 more source

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